Q9VR51 (Q9VR51_DROME) Unreviewed, UniProtKB/TrEMBL

Names and origin

Protein names

Submitted name:
CG14615 EMBL AAF50955.1

Submitted name:
RE68036p EMBL AAL49258.1

Gene names

ORF Names:

CG14615 FlyBase FBgn0031184 EMBL AAL49258.1, Dmel_CG14615 EMBL AAF50955.1

Organism

Drosophila melanogaster (Fruit fly) [Reference proteome]

Taxonomic identifier

7227 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Protostomia › Ecdysozoa › Panarthropoda › Arthropoda › Mandibulata › Pancrustacea › Hexapoda › Insecta › Dicondylia › Pterygota › Neoptera › Endopterygota › Diptera › Brachycera › Muscomorpha › Eremoneura › Cyclorrhapha › Schizophora › Acalyptratae › Ephydroidea › Drosophilidae › Drosophilinae › Drosophilini › Drosophilina › Drosophiliti › Drosophila › Sophophora › melanogaster group › melanogaster subgroup

Protein attributes

Sequence length	304 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

Ontologies

Keywords
Technical term	3D-structure PDB 1SQH Complete proteome Reference proteome
Gene Ontology (GO)
Molecular_function	transferase activity, transferring acyl groups other than amino-acyl groups Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequences

	Sequence		Length	Mass (Da)
	Q9VR51 [UniParc]. Last modified May 1, 2000. Version 1. Checksum: EBE225E5843B8D32	FASTA	304	34,836
	10 20 30 40 50 60 MSSDKNGDIL RPLSDSEVDE LLDLYKVKFG IRNFHYLLLY NQRKWDRQLS EAQIPRNDLN 70 80 90 100 110 120 HISLRKQFYT HRRGNFRTWG TYVSLHRDIV QSVSFFSWQP DGAAELWECL EQTQLIEWTQ 130 140 150 160 170 180 GALLTNVDLG FCNRVKELAV SRGVTAIQPR QCFGMVLSHE DAFCAKVPDL PSEFEIRRLR 190 200 210 220 230 240 AEDAAMVHDS WPNKGEGSLT YLQALVRFNK SLGICRSDTG ELIAWIFQND FSGLGMLQVL 250 260 270 280 290 300 PKAERRGLGG LLAAAMSREI ARGEEITLTA WIVATNWRSE ALLKRIGYQK DLVNEWIKLV PNSS

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The genome sequence of Drosophila melanogaster." Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., Sutton G.G., Wortman J.R., Yandell M.D. , Zhang Q., Chen L.X., Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J., Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C. Science 287:2185-2195(2000) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Berkeley.
[2]	Stapleton M., Brokstein P., Hong L., Agbayani A., Carlson J., Champe M., Chavez C., Dorsett V., Dresnek D., Farfan D., Frise E., George R., Gonzalez M., Guarin H., Kronmiller B., Li P., Liao G., Miranda A. , Mungall C.J., Nunoo J., Pacleb J., Paragas V., Park S., Patel S., Phouanenavong S., Wan K., Yu C., Lewis S.E., Rubin G.M., Celniker S. Submitted (DEC-2001) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE. Strain: Berkeley EMBL AAL49258.1.
[3]	"Annotation of the Drosophila melanogaster euchromatic genome: a systematic review." Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., Bettencourt B.R., Celniker S.E., de Grey A.D.N.J. , Drysdale R.A., Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E. Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002) [PubMed] [Europe PMC] [Abstract] Cited for: GENOME REANNOTATION. Strain: Berkeley.
[4]	"X-RAY STRUCTURE OF DROSOPHILA MALONOGASTER PROTEIN Q9VR51 NORTHEAST STRUCTURAL GENOMICS CONSORTIUM TARGET FR87." Kuzin A.P., Chen Y., Forouhar F., Acton T.B., Xiao R., Cooper B., Ho C.K., Montelione G.T., Tong L., Hunt J.F. Submitted (MAR-2004) to the PDB data bank Cited for: X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS).
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AE014298 Genomic DNA. Translation: AAF50955.1.
AY071636 mRNA. Translation: AAL49258.1.

RefSeq

NP_608459.1. NM_134615.2.

UniGene

Dm.236.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1SQH	X-ray	2.00	A	1-304	[»]

SMR

Q9VR51. Positions 7-303.

ModBase

Search...

Protein-protein interaction databases

STRING

7227.FBpp0077061.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblMetazoa

FBtr0077369; FBpp0077061; FBgn0031184.

GeneID

33129.

KEGG

dme:Dmel_CG14615.

UCSC

CG14615-RA. d. melanogaster.

Organism-specific databases

FlyBase

FBgn0031184. CG14615.

Phylogenomic databases

eggNOG

NOG120310.

GeneTree

ENSGT00500000045135.

InParanoid

Q9VR51.

OMA

ELIAWIF.

OrthoDB

EOG4XGXFT.

Family and domain databases

Gene3D

3.40.630.30. 2 hits.

InterPro

IPR016181. Acyl_CoA_acyltransferase.
IPR013653. FR47.
[Graphical view]

Pfam

PF08445. FR47. 1 hit.
[Graphical view]

SUPFAM

SSF55729. Acyl_CoA_acyltransferase. 1 hit.

ProtoNet

Search...

Other

EvolutionaryTrace

Q9VR51.

GenomeRNAi

33129.

NextBio

782050.

Entry information

Entry name

Q9VR51_DROME

Accession

Primary (citable) accession number: Q9VR51

Entry history

Integrated into UniProtKB/TrEMBL:	May 1, 2000
Last sequence update:	May 1, 2000
Last modified:	May 1, 2013
This is version 81 of the entry and version 1 of the sequence. [Complete history]

Entry status

Unreviewed (UniProtKB/TrEMBL)